| UniProt ID | SLT2_YEAST | |
|---|---|---|
| UniProt AC | Q00772 | |
| Protein Name | Mitogen-activated protein kinase SLT2/MPK1 | |
| Gene Name | SLT2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 484 | |
| Subcellular Localization | ||
| Protein Description | Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the SLT2/MPK1 kinase which itself then phosphorylates and activates the transcription factor RLM1. Directly phosphorylates BCY1 upon TOR complex 1 (TORC1) inhibition.. | |
| Protein Sequence | MADKIERHTFKVFNQDFSVDKRFQLIKEIGHGAYGIVCSARFAEAAEDTTVAIKKVTNVFSKTLLCKRSLRELKLLRHFRGHKNITCLYDMDIVFYPDGSINGLYLYEELMECDMHQIIKSGQPLTDAHYQSFTYQILCGLKYIHSADVLHRDLKPGNLLVNADCQLKICDFGLARGYSENPVENSQFLTEYVATRWYRAPEIMLSYQGYTKAIDVWSAGCILAEFLGGKPIFKGKDYVNQLNQILQVLGTPPDETLRRIGSKNVQDYIHQLGFIPKVPFVNLYPNANSQALDLLEQMLAFDPQKRITVDEALEHPYLSIWHDPADEPVCSEKFEFSFESVNDMEDLKQMVIQEVQDFRLFVRQPLLEEQRQLQLQQQQQQQQQQQQQQQQPSDVDNGNAAASEENYPKQMATSNSVAPQQESFGIHSQNLPRHDADFPPRPQESMMEMRPATGNTADIPPQNDNGTLLDLEKELEFGLDRKYF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 21 | Acetylation | NQDFSVDKRFQLIKE CCCCCHHHHHHHHHH | 53.62 | 24489116 | |
| 49 | Phosphorylation | FAEAAEDTTVAIKKV HHHHHCCCEEHHHHH | 18.06 | 28889911 | |
| 50 | Phosphorylation | AEAAEDTTVAIKKVT HHHHCCCEEHHHHHH | 21.91 | 28889911 | |
| 155 | Ubiquitination | DVLHRDLKPGNLLVN CEECCCCCCCCEEEC | 55.99 | 23749301 | |
| 178 | Phosphorylation | DFGLARGYSENPVEN HHHCCCCCCCCCCCC | 13.78 | 28889911 | |
| 179 | Phosphorylation | FGLARGYSENPVENS HHCCCCCCCCCCCCC | 33.45 | 28889911 | |
| 186 | Phosphorylation | SENPVENSQFLTEYV CCCCCCCCHHHHHHH | 14.59 | 28889911 | |
| 190 | Phosphorylation | VENSQFLTEYVATRW CCCCHHHHHHHHHCH | 26.93 | 11875433 | |
| 192 | Phosphorylation | NSQFLTEYVATRWYR CCHHHHHHHHHCHHC | 7.08 | 17330950 | |
| 195 | Phosphorylation | FLTEYVATRWYRAPE HHHHHHHHCHHCCCH | 16.22 | 27017623 | |
| 251 | Phosphorylation | QILQVLGTPPDETLR HHHHHHCCCCHHHHH | 27.73 | 28889911 | |
| 263 | Ubiquitination | TLRRIGSKNVQDYIH HHHHHCCCCHHHHHH | 56.79 | 23749301 | |
| 277 | Ubiquitination | HQLGFIPKVPFVNLY HHCCCCCCCCCCCCC | 58.69 | 17644757 | |
| 340 | Phosphorylation | KFEFSFESVNDMEDL CEEEEEECCCCHHHH | 24.98 | 28889911 | |
| 413 | Phosphorylation | NYPKQMATSNSVAPQ CCCCHHHCCCCCCCC | 24.09 | 28889911 | |
| 414 | Phosphorylation | YPKQMATSNSVAPQQ CCCHHHCCCCCCCCH | 19.98 | 28889911 | |
| 416 | Phosphorylation | KQMATSNSVAPQQES CHHHCCCCCCCCHHH | 21.30 | 23749301 | |
| 423 | Phosphorylation | SVAPQQESFGIHSQN CCCCCHHHCCCCCCC | 25.16 | 25752575 | |
| 428 | Phosphorylation | QESFGIHSQNLPRHD HHHCCCCCCCCCCCC | 20.88 | 19805511 | |
| 453 | Phosphorylation | MMEMRPATGNTADIP HHHCCCCCCCCCCCC | 33.38 | 28889911 | |
| 456 | Phosphorylation | MRPATGNTADIPPQN CCCCCCCCCCCCCCC | 27.35 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SLT2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 190 | T | Phosphorylation |
| 19779198 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of SLT2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-428, ANDMASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-190 AND TYR-192, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, AND MASSSPECTROMETRY. | |
